Table 2 Crystallographic data collection and refinement statistics.
From: Structural basis of IL-23 antagonism by an Alphabody protein scaffold
Crystal form 1 | Crystal form 2 | |
|---|---|---|
Data collection | ||
Space group | P1211 | P41212 |
Unit cell dimensions | ||
a, b, c (Å) | 56.96 56.74 100.07 | 57.85 57.85 366.48 |
α β γ (°) | 90, 99.73, 90 | 90, 90, 90 |
Resolution (Å) | 41–1.74 (1.85–1.74) | 57–3.4 (3.5–3.4) |
Rmeas (%) | 5.4 (63.6) | 11.6 (92.1) |
<I/σ(I)> | 13.7 (1.8) | 20.7 (5.2) |
Completeness (%) | 97.9 (91.1) | 99.85 (100.0) |
Redundancy | 3.4 (3.4) | 22.3 (23.4) |
Refinement | ||
Resolution (Å) | 40–1.7 | 57–3.4 |
No. of reflections | 213960 (32767) | 212910 (9551) |
Rwork/Rfree | 0.17/0.22 (0.27/0.33) | 0.26/0.29 (0.34/0.38) |
No. of atoms* | ||
Protein | 4,295 | 4,060 |
Ligand/ion/glycan | 35/2/61 | −/−/60 |
Water | 410 | — |
B-factors (Å2)* | ||
Protein | 38.7 | 116.3 |
Ligand/ion/glycan | 62.9/39.7/34.4 | −/−/104.6 |
Water | 41.6 | — |
R.m.s.d. | ||
Bond lengths (Å) | 0.007 | 0.005 |
Bond angles (°) | 1.04 | 1.1 |
